PhD student in Biochemistry
Université de Montréal
Award-winning publication: Maintenance of Native-like Protein Dynamics May Not Be Required for Engineering Functional Proteins
Published in: Chemistry & Biology
"Until very recently, proteins were perceived as inherently rigid entities. This perception gave rise to several fundamental issues when explaining their function and capacity to adapt. However, new evidence suggests that proteins are, in fact, flexible and dynamic. Our research explores the links between the function and dynamic of bacterial resistance proteins. The model is especially interesting since these proteins evolve very quickly to enable bacterial survival in the presence of new antibiotics. We revealed that two bacterial resistance proteins that are structurally and functionally similar also had a comparable dynamic pattern, therefore suggesting that protein flexibility is a basic property. Still, this flexibility may be altered when changing the protein sequence without modifying the structure or function. This surprising finding establishes the proteins' mutation tolerance."
The emergence of superbugs and the few new antibiotics that have been released call into question our concept of the function and adaptation capacity of bacterial resistance proteins. Furthermore, several of the antibiotics that are commonly administered were designed based on a static protein model that does not account for movement. Sophie Gobeil's research serves to elucidate protein function. Considering these findings in antibiotics design could lead to the development of a molecule that better fits the protein's different shapes and provides increased efficiency.